Q8WYB5 (KAT6B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase KAT6B
EC=2.3.1.48

Alternative name(s):
Histone acetyltransferase MOZ2
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4
Short name=MYST-4
Monocytic leukemia zinc finger protein-related factor

Gene names

Name:	KAT6B
Synonyms:	KIAA0383, MORF, MOZ2, MYST4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2073 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Ref.1 Ref.7 Ref.8
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.1
Subunit structure	Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with RUNX1 and RUNX2. Ref.7 Ref.8 Ref.9
Subcellular location	Nucleus Probable.
Tissue specificity	Ubiquitously expressed, with high levels in heart, pancreas, testis and ovary. Ref.1
Domain	The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression. Ref.1
Post-translational modification	Autoacetylated. Autoacetylation at Lys-815 is required for proper function By similarity.
Involvement in disease	A chromosomal aberration involving KAT6B may be a cause acute myeloid leukemias. Translocation t(10;16)(q22;p13) with CREBBP. Ohdo syndrome, SBBYS variant (SBBYSS) [MIM:603736]: A syndrome characterized by distinctive facial appearance with severe blepharophimosis, an immobile mask-like face, a bulbous nasal tip, and a small mouth with a thin upper lip. The condition presents in infancy with severe hypotonia and feeding problems. Associated skeletal problems include joint laxity, abnormally long thumbs and great toes, and dislocated or hypoplastic patellae. Structural cardiac defects are present in around 50% of cases, and dental anomalies, including small and pointed teeth, are common. Many affected individuals have abnormalities of thyroid structure or function. SBBYSS is usually associated with severe mental retardation, delayed motor milestones, and significantly impaired speech. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Genitopatellar syndrome (GTPTS) [MIM:606170]: A rare disorder consisting of microcephaly, severe psychomotor retardation, and characteristic coarse facial features, including broad nose and small or retracted chin, associated with congenital flexion contractures of the lower extremities, abnormal or missing patellae, and urogenital anomalies. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12
Sequence similarities	Belongs to the MYST (SAS/MOZ) family. Contains 1 C2HC-type zinc finger. Contains 1 H15 (linker histone H1/H5 globular) domain. Contains 2 PHD-type zinc fingers.
Sequence caution	The sequence AAF00100.1 differs from that shown. Reason: Frameshift at positions 550 and 562. The sequence AAH14143.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH48199.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Acyltransferase Chromatin regulator Repressor Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 acetylation Inferred from direct assay Ref.8. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.1. Source: UniProtKB nucleosome assembly Non-traceable author statement Ref.1. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.1Ref.7. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MOZ/MORF histone acetyltransferase complex Inferred from direct assay Ref.8Ref.9. Source: UniProtKB nucleosome Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro histone acetyltransferase activity Inferred from direct assay Ref.1. Source: UniProtKB transcription factor binding Inferred from direct assay Ref.7. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8WYB5-1)

Also known as: Beta;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8WYB5-2)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     482-664: Missing.

Isoform 3 (identifier: Q8WYB5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     373-664: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2073	2073	Histone acetyltransferase KAT6B		PRO_0000051575
Regions
	Domain	103 – 176	74	H15
	Zinc finger	213 – 272	60	PHD-type 1
	Zinc finger	269 – 320	52	PHD-type 2
	Zinc finger	749 – 771	23	C2HC-type
	Region	361 – 717	357	Negatively regulates HAT activity
	Region	718 – 1008	291	Catalytic
	Region	752 – 1008	257	Interaction with BRPF1
	Region	856 – 860	5	Acetyl-CoA binding By similarity
	Region	865 – 871	7	Acetyl-CoA binding By similarity
	Region	1560 – 2073	514	Interaction with RUNX1 and RUNX2
	Compositional bias	492 – 533	42	Ser-rich
	Compositional bias	521 – 524	4	Poly-Ser
	Compositional bias	599 – 605	7	Poly-Ser
	Compositional bias	1070 – 1104	35	Poly-Glu
	Compositional bias	1204 – 1207	4	Poly-Glu
	Compositional bias	1351 – 1373	23	Poly-Glu
	Compositional bias	1409 – 1417	9	Poly-Glu
	Compositional bias	1594 – 1763	170	Ser-rich
	Compositional bias	1961 – 2061	101	Met-rich
Sites
	Active site	815	1	By similarity
	Active site	857	1	Nucleophile By similarity
	Binding site	895	1	Acetyl-CoA By similarity
	Site	1222 – 1223	2	Breakpoint for translocation to form KAT6B-CREBBP
Amino acid modifications
	Modified residue	815	1	N6-acetyllysine; by autocatalysis By similarity
	Modified residue	1038	1	N6-acetyllysine Ref.10
	Modified residue	1042	1	N6-acetyllysine Ref.10
	Modified residue	1044	1	N6-acetyllysine Ref.10
Natural variations
	Alternative sequence	373 – 664	292	Missing in isoform 3.		VSP_014586
	Alternative sequence	482 – 664	183	Missing in isoform 2.		VSP_014587
	Natural variant	360	1	E → K. Ref.11		VAR_067315
	Natural variant	483	1	T → A in a breast cancer sample; somatic mutation. Ref.13		VAR_036361
	Natural variant	1217	1	A → S. Corresponds to variant rs57372986 [ dbSNP | Ensembl ].		VAR_061367
	Natural variant	1499	1	V → I. Corresponds to variant rs3740321 [ dbSNP | Ensembl ].		VAR_050217
Experimental info
	Sequence conflict	123	1	G → R in AAL56647. Ref.2
	Sequence conflict	231	1	P → A in AAL56647. Ref.2
	Sequence conflict	843	1	F → L in AAF00095. Ref.1
	Sequence conflict	843	1	F → L in AAF00099. Ref.1
	Sequence conflict	843	1	F → L in AAF00100. Ref.1
	Sequence conflict	843	1	F → L in BAA20837. Ref.3
	Sequence conflict	931 – 933	3	TGM → RHV in AAL56647. Ref.2
	Sequence conflict	934	1	Missing in AAL56647. Ref.2
	Sequence conflict	1152	1	T → S in AAL56647. Ref.2
	Sequence conflict	1625	1	S → T in AAL56647. Ref.2
	Sequence conflict	1731	1	S → T in AAL56647. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Beta) [UniParc]. Last modified April 3, 2007. Version 3. Checksum: AEE267B9DA444B08	FASTA	2,073	231,378
	10 20 30 40 50 60 MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ LELSVQDGSV 70 80 90 100 110 120 LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK SAKGSRGSCN DLRNVDWNKL LRRAIEGLEE 130 140 150 160 170 180 PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGSLD 190 200 210 220 230 240 GKGAPQYPSA FPSSLPPVSL LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC 250 260 270 280 290 300 GSSGHPSCLK FCPELTTNVK ALRWQCIECK TCSACRVQGR NADNMLFCDS CDRGFHMECC 310 320 330 340 350 360 DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK QRLLSVTSDE 370 380 390 400 410 420 GSMNAFTGRG SPGRGQKTKV CTTPSSGHAA SGKDSSSRLA VTDPTRPGAT TKITTTSTYI 430 440 450 460 470 480 SASTLKVNKK TKGLIDGLTK FFTPSPDGRR SRGEIIDFSK HYRPRKKVSQ KQSCTSHVLA 490 500 510 520 530 540 TGTTQKLKPP PSSLPPPTPI SGQSPSSQKS STATSSPSPQ SSSSQCSVPS LSSLTTNSQL 550 560 570 580 590 600 KALFDGLSHI YTTQGQSRKK GHPSYAPPKR MRRKTELSST AKSKAHFFGK RDIRSRFISH 610 620 630 640 650 660 SSSSSWGMAR GSIFKAIAHF KRTTFLKKHR MLGRLKYKVT PQMGTPSPGK GSLTDGRIKP 670 680 690 700 710 720 DQDDDTEIKI NIKQESADVN VIGNKDVVTE EDLDVFKQAQ ELSWEKIECE SGVEDCGRYP 730 740 750 760 770 780 SVIEFGKYEI QTWYSSPYPQ EYARLPKLYL CEFCLKYMKS KNILLRHSKK CGWFHPPANE 790 800 810 820 830 840 IYRRKDLSVF EVDGNMSKIY CQNLCLLAKL FLDHKTLYYD VEPFLFYVLT KNDEKGCHLV 850 860 870 880 890 900 GYFSKEKLCQ QKYNVSCIMI MPQHQRQGFG RFLIDFSYLL SRREGQAGSP EKPLSDLGRL 910 920 930 940 950 960 SYLAYWKSVI LEYLYHHHER HISIKAISRA TGMCPHDIAT TLQHLHMIDK RDGRFVIIRR 970 980 990 1000 1010 1020 EKLILSHMEK LKTCSRANEL DPDSLRWTPI LISNAAVSEE EREAEKEAER LMEQASCWEK 1030 1040 1050 1060 1070 1080 EEQEILSTRA NSRQSPAKVQ SKNKYLHSPE SRPVTGERGQ LLELSKESSE EEEEEEDEEE 1090 1100 1110 1120 1130 1140 EEEEEEEEED EEEEEEEEEE EEEENIQSSP PRLTKPQSVA IKRKRPFVLK KKRGRKRRRI 1150 1160 1170 1180 1190 1200 NSSVTTETIS ETTEVLNEPF DNSDEERPMP QLEPTCEIEV EEDGRKPVLR KAFQHQPGKK 1210 1220 1230 1240 1250 1260 RQTEEEEGKD NHCFKNADPC RNNMNDDSSN LKEGSKDNPE PLKCKQVWPK GTKRGLSKWR 1270 1280 1290 1300 1310 1320 QNKERKTGFK LNLYTPPETP MEPDEQVTVE EQKETSEGKT SPSPIRIEEE VKETGEALLP 1330 1340 1350 1360 1370 1380 QEENRREETC APVSPNTSPG EKPEDDLIKP EEEEEEEEEE EEEEEEEEGE EEEGGGNVEK 1390 1400 1410 1420 1430 1440 DPDGAKSQEK EEPEISTEKE DSARLDDHEE EEEEDEEPSH NEDHDADDED DSHMESAEVE 1450 1460 1470 1480 1490 1500 KEELPRESFK EVLENQETFL DLNVQPGHSN PEVLMDCGVD LTASCNSEPK ELAGDPEAVP 1510 1520 1530 1540 1550 1560 ESDEEPPPGE QAQKQDQKNS KEVDTEFKEG NPATMEIDSE TVQAVQSLTQ ESSEQDDTFQ 1570 1580 1590 1600 1610 1620 DCAETQEACR SLQNYTRADQ SPQIATTLDD CQQSDHSSPV SSVHSHPGQS VRSVNSPSVP 1630 1640 1650 1660 1670 1680 ALENSYAQIS PDQSAISVPS LQNMETSPMM DVPSVSDHSQ QVVDSGFSDL GSIESTTENY 1690 1700 1710 1720 1730 1740 ENPSSYDSTM GGSICGNGSS QNSCSYSNLT SSSLTQSSCA VTQQMSNISG SCSMLQQTSI 1750 1760 1770 1780 1790 1800 SSPPTCSVKS PQGCVVERPP SSSQQLAQCS MAANFTPPMQ LAEIPETSNA NIGLYERMGQ 1810 1820 1830 1840 1850 1860 SDFGAGHYPQ PSATFSLAKL QQLTNTLIDH SLPYSHSAAV TSYANSASLS TPLSNTGLVQ 1870 1880 1890 1900 1910 1920 LSQSPHSVPG GPQAQATMTP PPNLTPPPMN LPPPLLQRNM AASNIGISHS QRLQTQIASK 1930 1940 1950 1960 1970 1980 GHISMRTKSA SLSPAAATHQ SQIYGRSQTV AMQGPARTLT MQRGMNMSVN LMPAPAYNVN 1990 2000 2010 2020 2030 2040 SVNMNMNTLN AMNGYSMSQP MMNSGYHSNH GYMNQTPQYP MQMQMGMMGT QPYAQQPMQT 2050 2060 2070 PPHGNMMYTA PGHHGYMNTG MSKQSLNGSY MRR
	Isoform 2 (Alpha) [UniParc]. Checksum: 9AD95D653693CFBA	FASTA	1,890	211,537
	10 20 30 40 50 60 MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ LELSVQDGSV 70 80 90 100 110 120 LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK SAKGSRGSCN DLRNVDWNKL LRRAIEGLEE 130 140 150 160 170 180 PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGSLD 190 200 210 220 230 240 GKGAPQYPSA FPSSLPPVSL LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC 250 260 270 280 290 300 GSSGHPSCLK FCPELTTNVK ALRWQCIECK TCSACRVQGR NADNMLFCDS CDRGFHMECC 310 320 330 340 350 360 DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK QRLLSVTSDE 370 380 390 400 410 420 GSMNAFTGRG SPGRGQKTKV CTTPSSGHAA SGKDSSSRLA VTDPTRPGAT TKITTTSTYI 430 440 450 460 470 480 SASTLKVNKK TKGLIDGLTK FFTPSPDGRR SRGEIIDFSK HYRPRKKVSQ KQSCTSHVLA 490 500 510 520 530 540 TDTEIKINIK QESADVNVIG NKDVVTEEDL DVFKQAQELS WEKIECESGV EDCGRYPSVI 550 560 570 580 590 600 EFGKYEIQTW YSSPYPQEYA RLPKLYLCEF CLKYMKSKNI LLRHSKKCGW FHPPANEIYR 610 620 630 640 650 660 RKDLSVFEVD GNMSKIYCQN LCLLAKLFLD HKTLYYDVEP FLFYVLTKND EKGCHLVGYF 670 680 690 700 710 720 SKEKLCQQKY NVSCIMIMPQ HQRQGFGRFL IDFSYLLSRR EGQAGSPEKP LSDLGRLSYL 730 740 750 760 770 780 AYWKSVILEY LYHHHERHIS IKAISRATGM CPHDIATTLQ HLHMIDKRDG RFVIIRREKL 790 800 810 820 830 840 ILSHMEKLKT CSRANELDPD SLRWTPILIS NAAVSEEERE AEKEAERLME QASCWEKEEQ 850 860 870 880 890 900 EILSTRANSR QSPAKVQSKN KYLHSPESRP VTGERGQLLE LSKESSEEEE EEEDEEEEEE 910 920 930 940 950 960 EEEEEEDEEE EEEEEEEEEE ENIQSSPPRL TKPQSVAIKR KRPFVLKKKR GRKRRRINSS 970 980 990 1000 1010 1020 VTTETISETT EVLNEPFDNS DEERPMPQLE PTCEIEVEED GRKPVLRKAF QHQPGKKRQT 1030 1040 1050 1060 1070 1080 EEEEGKDNHC FKNADPCRNN MNDDSSNLKE GSKDNPEPLK CKQVWPKGTK RGLSKWRQNK 1090 1100 1110 1120 1130 1140 ERKTGFKLNL YTPPETPMEP DEQVTVEEQK ETSEGKTSPS PIRIEEEVKE TGEALLPQEE 1150 1160 1170 1180 1190 1200 NRREETCAPV SPNTSPGEKP EDDLIKPEEE EEEEEEEEEE EEEEEGEEEE GGGNVEKDPD 1210 1220 1230 1240 1250 1260 GAKSQEKEEP EISTEKEDSA RLDDHEEEEE EDEEPSHNED HDADDEDDSH MESAEVEKEE 1270 1280 1290 1300 1310 1320 LPRESFKEVL ENQETFLDLN VQPGHSNPEV LMDCGVDLTA SCNSEPKELA GDPEAVPESD 1330 1340 1350 1360 1370 1380 EEPPPGEQAQ KQDQKNSKEV DTEFKEGNPA TMEIDSETVQ AVQSLTQESS EQDDTFQDCA 1390 1400 1410 1420 1430 1440 ETQEACRSLQ NYTRADQSPQ IATTLDDCQQ SDHSSPVSSV HSHPGQSVRS VNSPSVPALE 1450 1460 1470 1480 1490 1500 NSYAQISPDQ SAISVPSLQN METSPMMDVP SVSDHSQQVV DSGFSDLGSI ESTTENYENP 1510 1520 1530 1540 1550 1560 SSYDSTMGGS ICGNGSSQNS CSYSNLTSSS LTQSSCAVTQ QMSNISGSCS MLQQTSISSP 1570 1580 1590 1600 1610 1620 PTCSVKSPQG CVVERPPSSS QQLAQCSMAA NFTPPMQLAE IPETSNANIG LYERMGQSDF 1630 1640 1650 1660 1670 1680 GAGHYPQPSA TFSLAKLQQL TNTLIDHSLP YSHSAAVTSY ANSASLSTPL SNTGLVQLSQ 1690 1700 1710 1720 1730 1740 SPHSVPGGPQ AQATMTPPPN LTPPPMNLPP PLLQRNMAAS NIGISHSQRL QTQIASKGHI 1750 1760 1770 1780 1790 1800 SMRTKSASLS PAAATHQSQI YGRSQTVAMQ GPARTLTMQR GMNMSVNLMP APAYNVNSVN 1810 1820 1830 1840 1850 1860 MNMNTLNAMN GYSMSQPMMN SGYHSNHGYM NQTPQYPMQM QMGMMGTQPY AQQPMQTPPH 1870 1880 1890 GNMMYTAPGH HGYMNTGMSK QSLNGSYMRR
	Isoform 3 [UniParc]. Checksum: 895F7DE8B12455E8	FASTA	1,781	199,858
	10 20 30 40 50 60 MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ LELSVQDGSV 70 80 90 100 110 120 LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK SAKGSRGSCN DLRNVDWNKL LRRAIEGLEE 130 140 150 160 170 180 PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGSLD 190 200 210 220 230 240 GKGAPQYPSA FPSSLPPVSL LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC 250 260 270 280 290 300 GSSGHPSCLK FCPELTTNVK ALRWQCIECK TCSACRVQGR NADNMLFCDS CDRGFHMECC 310 320 330 340 350 360 DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK QRLLSVTSDE 370 380 390 400 410 420 GSMNAFTGRG SPDTEIKINI KQESADVNVI GNKDVVTEED LDVFKQAQEL SWEKIECESG 430 440 450 460 470 480 VEDCGRYPSV IEFGKYEIQT WYSSPYPQEY ARLPKLYLCE FCLKYMKSKN ILLRHSKKCG 490 500 510 520 530 540 WFHPPANEIY RRKDLSVFEV DGNMSKIYCQ NLCLLAKLFL DHKTLYYDVE PFLFYVLTKN 550 560 570 580 590 600 DEKGCHLVGY FSKEKLCQQK YNVSCIMIMP QHQRQGFGRF LIDFSYLLSR REGQAGSPEK 610 620 630 640 650 660 PLSDLGRLSY LAYWKSVILE YLYHHHERHI SIKAISRATG MCPHDIATTL QHLHMIDKRD 670 680 690 700 710 720 GRFVIIRREK LILSHMEKLK TCSRANELDP DSLRWTPILI SNAAVSEEER EAEKEAERLM 730 740 750 760 770 780 EQASCWEKEE QEILSTRANS RQSPAKVQSK NKYLHSPESR PVTGERGQLL ELSKESSEEE 790 800 810 820 830 840 EEEEDEEEEE EEEEEEEDEE EEEEEEEEEE EENIQSSPPR LTKPQSVAIK RKRPFVLKKK 850 860 870 880 890 900 RGRKRRRINS SVTTETISET TEVLNEPFDN SDEERPMPQL EPTCEIEVEE DGRKPVLRKA 910 920 930 940 950 960 FQHQPGKKRQ TEEEEGKDNH CFKNADPCRN NMNDDSSNLK EGSKDNPEPL KCKQVWPKGT 970 980 990 1000 1010 1020 KRGLSKWRQN KERKTGFKLN LYTPPETPME PDEQVTVEEQ KETSEGKTSP SPIRIEEEVK 1030 1040 1050 1060 1070 1080 ETGEALLPQE ENRREETCAP VSPNTSPGEK PEDDLIKPEE EEEEEEEEEE EEEEEEGEEE 1090 1100 1110 1120 1130 1140 EGGGNVEKDP DGAKSQEKEE PEISTEKEDS ARLDDHEEEE EEDEEPSHNE DHDADDEDDS 1150 1160 1170 1180 1190 1200 HMESAEVEKE ELPRESFKEV LENQETFLDL NVQPGHSNPE VLMDCGVDLT ASCNSEPKEL 1210 1220 1230 1240 1250 1260 AGDPEAVPES DEEPPPGEQA QKQDQKNSKE VDTEFKEGNP ATMEIDSETV QAVQSLTQES 1270 1280 1290 1300 1310 1320 SEQDDTFQDC AETQEACRSL QNYTRADQSP QIATTLDDCQ QSDHSSPVSS VHSHPGQSVR 1330 1340 1350 1360 1370 1380 SVNSPSVPAL ENSYAQISPD QSAISVPSLQ NMETSPMMDV PSVSDHSQQV VDSGFSDLGS 1390 1400 1410 1420 1430 1440 IESTTENYEN PSSYDSTMGG SICGNGSSQN SCSYSNLTSS SLTQSSCAVT QQMSNISGSC 1450 1460 1470 1480 1490 1500 SMLQQTSISS PPTCSVKSPQ GCVVERPPSS SQQLAQCSMA ANFTPPMQLA EIPETSNANI 1510 1520 1530 1540 1550 1560 GLYERMGQSD FGAGHYPQPS ATFSLAKLQQ LTNTLIDHSL PYSHSAAVTS YANSASLSTP 1570 1580 1590 1600 1610 1620 LSNTGLVQLS QSPHSVPGGP QAQATMTPPP NLTPPPMNLP PPLLQRNMAA SNIGISHSQR 1630 1640 1650 1660 1670 1680 LQTQIASKGH ISMRTKSASL SPAAATHQSQ IYGRSQTVAM QGPARTLTMQ RGMNMSVNLM 1690 1700 1710 1720 1730 1740 PAPAYNVNSV NMNMNTLNAM NGYSMSQPMM NSGYHSNHGY MNQTPQYPMQ MQMGMMGTQP 1750 1760 1770 1780 YAQQPMQTPP HGNMMYTAPG HHGYMNTGMS KQSLNGSYMR R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein." Champagne N., Bertos N.R., Pelletier N., Wang A.H., Vezmar M., Yang Y., Heng H.H., Yang X.-J. J. Biol. Chem. 274:28528-28536(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, ACETYLATION, ENZYME ACTIVITY, DOMAIN, FUNCTION. Tissue: Bone marrow.
[2]	"Structure and function of the human MYST family: MOZ2, MYST1 and MYST2." Borrow J., Housman D.E. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[4]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-322 AND 1187-2073. Tissue: Brain and Lung.
[6]	"Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13)." Panagopoulos I., Fioretos T., Isaksson M., Samuelsson U., Billstroem R., Stroembeck B., Mitelman F., Johansson B. Hum. Mol. Genet. 10:395-404(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1136-1287, CHROMOSOMAL TRANSLOCATION WITH CREBBP.
[7]	"MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2." Pelletier N., Champagne N., Stifani S., Yang X.-J. Oncogene 21:2729-2740(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RUNX1 AND RUNX2, ACETYLATION, FUNCTION.
[8]	"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation." Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J. Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
[9]	"Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes." Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C., Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J., Yang X.-J. Mol. Cell. Biol. 28:6828-6843(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1038; LYS-1042 AND LYS-1044, MASS SPECTROMETRY.
[11]	"Whole-exome-sequencing identifies mutations in histone acetyltransferase gene KAT6B in individuals with the Say-Barber-Biesecker variant of Ohdo syndrome." Clayton-Smith J., O'Sullivan J., Daly S., Bhaskar S., Day R., Anderson B., Voss A.K., Thomas T., Biesecker L.G., Smith P., Fryer A., Chandler K.E., Kerr B., Tassabehji M., Lynch S.A., Krajewska-Walasek M., McKee S., Smith J. , Sweeney E., Mansour S., Mohammed S., Donnai D., Black G. Am. J. Hum. Genet. 89:675-681(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SBBYSS, VARIANT LYS-360.
[12]	"Mutations in KAT6B, encoding a histone acetyltransferase, cause Genitopatellar syndrome." Campeau P.M., Kim J.C., Lu J.T., Schwartzentruber J.A., Abdul-Rahman O.A., Schlaubitz S., Murdock D.M., Jiang M.M., Lammer E.J., Enns G.M., Rhead W.J., Rowland J., Robertson S.P., Cormier-Daire V., Bainbridge M.N., Yang X.J., Gingras M.C., Gibbs R.A. , Rosenblatt D.S., Majewski J., Lee B.H. Am. J. Hum. Genet. 90:282-289(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN GTPTS.
[13]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-483.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF113514 mRNA. Translation: AAF00095.1. AF119230 mRNA. Translation: AAF00099.1. AF119231 mRNA. Translation: AAF00100.1. Frameshift. AF217500 mRNA. Translation: AAL56647.1. AB002381 mRNA. Translation: BAA20837.2. BC014143 mRNA. Translation: AAH14143.1. Sequence problems. BC021128 mRNA. Translation: AAH21128.1. BC048199 mRNA. Translation: AAH48199.1. Sequence problems.
IPI	IPI00099433. IPI00384388. IPI00607795.
RefSeq	NP_001243397.1. NM_001256468.1. NP_001243398.1. NM_001256469.1. NP_036462.2. NM_012330.3.
UniGene	Hs.35758. Hs.599543. Hs.740873.
3D structure databases
ProteinModelPortal	Q8WYB5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8WYB5. 3 interactions.
MINT	MINT-2871056.
STRING	9606.ENSP00000287239.
PTM databases
PhosphoSite	Q8WYB5.
Polymorphism databases
DMDM	143811424.
Proteomic databases
PaxDb	Q8WYB5.
PRIDE	Q8WYB5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000287239; ENSP00000287239; ENSG00000156650. ENST00000372711; ENSP00000361796; ENSG00000156650. ENST00000372714; ENSP00000361799; ENSG00000156650. ENST00000372724; ENSP00000361809; ENSG00000156650. ENST00000372725; ENSP00000361810; ENSG00000156650.
GeneID	23522.
KEGG	hsa:23522.
UCSC	uc001jwn.1. human. uc001jwo.1. human. uc001jwp.1. human.
Organism-specific databases
CTD	23522.
GeneCards	GC10P076586.
HGNC	HGNC:17582. KAT6B.
HPA	HPA006104.
MIM	603736. phenotype. 605880. gene. 606170. phenotype.
neXtProt	NX_Q8WYB5.
Orphanet	3047. Blepharophimosis-intellectual deficit syndrome, SBBYS type. 85201. Genitopatellar syndrome. 648. Noonan syndrome.
PharmGKB	PA134880712.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5027.
HOVERGEN	HBG052563.
InParanoid	Q8WYB5.
KO	K11306.
OMA	KRKRPFV.
PhylomeDB	Q8WYB5.
Enzyme and pathway databases
BRENDA	2.3.1.48. 2681.
Gene expression databases
ArrayExpress	Q8WYB5.
Bgee	Q8WYB5.
CleanEx	HS_MYST4.
Genevestigator	Q8WYB5.
GermOnline	ENSG00000156650. Homo sapiens.
Family and domain databases
Gene3D	1.10.10.10. 1 hit. 3.30.40.10. 1 hit. 3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR005818. Histone_H1/H5. IPR002717. MOZ_SAS. IPR011991. WHTH_DNA-bd_dom. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF00538. Linker_histone. 1 hit. PF01853. MOZ_SAS. 1 hit. PF00628. PHD. 1 hit. [Graphical view]
SMART	SM00526. H15. 1 hit. SM00249. PHD. 2 hits. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS51504. H15. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	KAT6B. human.
GenomeRNAi	23522.
NextBio	45977.
SOURCE	Search...

Entry information

Entry name

KAT6B_HUMAN

Accession

Primary (citable) accession number: Q8WYB5
Secondary accession number(s): O15087 , Q86Y05, Q8WU81, Q9UKW2, Q9UKW3, Q9UKX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.